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Transduced HSP27 protein protects neuronal cell death by enhancing FALS-associated SOD1 mutant activity

  • An, Jae-Jin (Department of Biomedical Science and Research Institute for Bioscience and Biotechnology, Hallym University) ;
  • Lee, Yeom-Pyo (Department of Biomedical Science and Research Institute for Bioscience and Biotechnology, Hallym University) ;
  • Kim, Dae-Won (Department of Biomedical Science and Research Institute for Bioscience and Biotechnology, Hallym University) ;
  • Sohn, Eun-Joung (Department of Biomedical Science and Research Institute for Bioscience and Biotechnology, Hallym University) ;
  • Jeong, Hoon-Jae (Department of Biomedical Science and Research Institute for Bioscience and Biotechnology, Hallym University) ;
  • Kang, Hye-Won (Department of Biomedical Science and Research Institute for Bioscience and Biotechnology, Hallym University) ;
  • Shin, Min-Jae (Department of Biomedical Science and Research Institute for Bioscience and Biotechnology, Hallym University) ;
  • Kim, Mi-Jin (Department of Biomedical Science and Research Institute for Bioscience and Biotechnology, Hallym University) ;
  • Ahn, Eun-Hee (Department of Biomedical Science and Research Institute for Bioscience and Biotechnology, Hallym University) ;
  • Jang, Sang-Ho (Department of Biomedical Science and Research Institute for Bioscience and Biotechnology, Hallym University) ;
  • Kang, Jung-Hoon (Department of Genetic Engineering, Cheongju University) ;
  • Kang, Tae-Cheon (Department of Anatomy and Neurobiology, College of Medicine, Hallym University) ;
  • Won, Moo-Ho (Department of Anatomy and Neurobiology, College of Medicine, Hallym University) ;
  • Kwon, Oh-Shin (Department of Biochemistry, Kyungpook National University) ;
  • Cho, Sung-Woo (Department of Biochemistry and Molecular Biology, University of Ulsan College of Medicine) ;
  • Lee, Kil-Soo (Department of Biomedical Science and Research Institute for Bioscience and Biotechnology, Hallym University) ;
  • Park, Jin-Seu (Department of Biomedical Science and Research Institute for Bioscience and Biotechnology, Hallym University) ;
  • Eum, Won-Sik (Department of Biomedical Science and Research Institute for Bioscience and Biotechnology, Hallym University) ;
  • Choi, Soo-Young (Department of Biomedical Science and Research Institute for Bioscience and Biotechnology, Hallym University)
  • Published : 2009.03.31
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Abstract

Familial Amyotrophic lateral sclerosis (FALS) is a progressive neurodegenetative disorder induced by mutations of the SOD1 gene. Heat shock protein 27 (HSP27) is well-defined as a stress-inducible protein, however the its role in ALS protection has not yet been established. To investigate the role HSP27 may have in SOD1 mutant-mediated apoptosis, human SOD1 or HSP27 genes were fused with a PEP-1 peptide in a bacterial expression vector to produce a genetic in-frame fusion protein, which was then transduced into cells. We found the purified PEP-1-HSP27 fusion proteins can be transduced efficiently into neuronal cells and protect against cell death by enhancing mutant SOD1 activity. Moreover, transduced PEP-1-HSP27 efficiently prevents protein aggregation produced by oxidative stress. These results suggest that transduced HSP27 fusion protein may be explored as a potential therapeutic agent for FALS patients.

Keywords

References

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